3IWX
Crystal structure of cisplatin bound to a human copper chaperone (dimer)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005507 | molecular_function | copper ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0006811 | biological_process | monoatomic ion transport |
| A | 0006825 | biological_process | copper ion transport |
| A | 0006878 | biological_process | intracellular copper ion homeostasis |
| A | 0006979 | biological_process | response to oxidative stress |
| A | 0016530 | molecular_function | metallochaperone activity |
| A | 0016531 | molecular_function | copper chaperone activity |
| A | 0032767 | molecular_function | copper-dependent protein binding |
| A | 0043066 | biological_process | negative regulation of apoptotic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051117 | molecular_function | ATPase binding |
| A | 0060003 | biological_process | copper ion export |
| A | 1903136 | molecular_function | cuprous ion binding |
| B | 0005507 | molecular_function | copper ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0006811 | biological_process | monoatomic ion transport |
| B | 0006825 | biological_process | copper ion transport |
| B | 0006878 | biological_process | intracellular copper ion homeostasis |
| B | 0006979 | biological_process | response to oxidative stress |
| B | 0016530 | molecular_function | metallochaperone activity |
| B | 0016531 | molecular_function | copper chaperone activity |
| B | 0032767 | molecular_function | copper-dependent protein binding |
| B | 0043066 | biological_process | negative regulation of apoptotic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051117 | molecular_function | ATPase binding |
| B | 0060003 | biological_process | copper ion export |
| B | 1903136 | molecular_function | cuprous ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CPT A 69 |
| Chain | Residue |
| A | THR11 |
| A | CYS12 |
| A | CYS15 |
| B | THR11 |
| B | CYS12 |
| B | CYS15 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 71 |
| Chain | Residue |
| A | HIS46 |
| A | SER47 |
| A | THR50 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 70 |
| Chain | Residue |
| B | GLY28 |
| B | HOH96 |
| B | HOH114 |
| B | HOH126 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 71 |
| Chain | Residue |
| B | HIS46 |
| B | SER47 |
| B | THR50 |
| B | HOH91 |
| B | HOH120 |
Functional Information from PROSITE/UniProt
| site_id | PS01047 |
| Number of Residues | 29 |
| Details | HMA_1 Heavy-metal-associated domain. SvDMtCgGCaeaVSrvLnklggvkyd..IdL |
| Chain | Residue | Details |
| A | SER7-LEU35 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00280","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"31283225","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5T7L","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"O08997","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
